Crystal Structure of PKG I:cGMP Complex Reveals a cGMP-Mediated Dimeric Interface that Facilitates cGMP-Induced Activation
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- 作者：Jeong Joo Kim1 ; 2 ; Robin Lorenz2 ; Stefan T. Arold3 ; Albert S. Reger1 ; 7 ; Banumathi Sankaran4 ; Darren E. Casteel5 ; Friedrich W. Herberg2 ; Choel Kim1 ; 6 ; ckim@bcm.edu" class="auth_mail" title="E-mail the corresponding author
- 关键词：NO-cGMP signaling ; second messengers ; cGMP-dependent protein kinase ; cyclic nucleotide-binding domain ; allosteric activation ; crystal structure ; small-angle X-ray scattering
- 刊名：Structure
- 出版年：2016
- 出版时间：3 May 2016
- 年：2016
- 卷：24
- 期：5
- 页码：710-720
- 全文大小：3599 K
文摘
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Structure of monomeric PKG I R reveals a new dimeric interface mediated by cGMP
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Mutagenesis of the key interface residues reduces cGMP binding and activation
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SAXS analysis of the PKG I R dimer supports the cGMP-mediated dimer model
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The dimeric interface may acts as a “safety lock” to ensure kinase activation